This book describes the present state of knowledge regarding the impact of cyanobacteria on health through the use of water. It considers aspects of risk management and details the information needed for protecting drinking water sources and recreational water bodies from the health hazards caused by cyanobacteria and their toxins. It also outlines the state of knowledge regarding the principal considerations in the design of programmes and studies for monitoring water resources and supplies and describes the approaches and procedures used.
The development of this publication was guided by the recommendations of several expert meetings concerning drinking water (Geneva, December 1995; Bad Elster, June
1996) and recreational water (Bad Elster, June 1996; St Helier, May 1997). An expert meeting in Bad Elster, April 1997, critically reviewed the literature concerning the toxicity of cyanotoxins and developed the scope and content of this book. A draft manuscript was reviewed at an editorial meeting in November 1997, and a further draft was
reviewed by the working group responsible for updating the Guidelines for Drinkingwater Quality in March 1998.

/pdf/toxic-cyanobacteria-in-water-a-guide-to-their-public-health-2y64v55hv1.pdf

Toxic cyanobacteria in water: a guide to their public health consequences, monitoring and management.

Proposal for a common nomenclature for sequence ions in mass spectra of peptides.

Cyanobacteria secondary metabolites--the cyanotoxins.

Calcineurin is a eukaryotic Ca2+- and calmodulin-dependent serine/threonine protein phosphatase. It is a heterodimeric protein consisting of a catalytic subunit calcineurin A, which contains an act...

https://www.physiology.org/doi/pdf/10.1152/physrev.2000.80.4.1483

Calcineurin : form and function

Regulation of the Calmodulin-stimulated Protein Phosphatase, Calcineurin

The structure of cyanoginosin-LA (previously referred to by us as toxin BE-4) is cyclo(-D-Ala-L-Leu-erythro-β-methyl-D-isoAsp-L-Ala-Adda-D-Glu-N-methyldehydroAla)(17a), where Adda refers to the novel β-amino acid residue of 3-amino-9-methoxy-2,6,8-trimethyl-10-phenyldeca-4,6-dienoic acid (11). The connectivity of Adda is deduced from 1H- and 13C-n.m.r. data, but the stereochemistry at carbons 2,3,8, and 9 remains unknown. The residue sequence is derived from the mass spectra of cyclic and linear derivatives of the toxin. A new nomenclature for the related toxins of Microcystis aeruginosa is discussed.

The structure of cyanoginosin-LA, a cyclic heptapeptide toxin from the cyanobacterium Microcystis aeruginosa

https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/0014-5793%2882%2980759-X

Identification of the NH2‐terminal blocking group of calcineurin B as myristic acid

A study of a range of polar organic molecules by fast atom bombardment (FAB) mass spectrometry is reported Compounds studied include organic salts, polar antibiotics, nucleoside phosphates, and underivatized peptides In these classes of compounds, molecular weights in the range 300 to 2000 daltons have been routinely determined, operating in both positive and negative ion modes Molecular weights of peptides are readily obtained on less than 1 nmol of material, and sequence information is conveniently deduced from sample sizes in the range 2 to 50 nmol

Fast atom bombardment mass spectrometry: a powerful technique for the study of polar molecules

The structures of the hepatotoxins of general name cyanoginosins-XY are proposed to be cyclo-D-Ala-L-X-erythro-β-methyl-D-isoAsp-L-Y-Adda-D-isoGlu-N-methyldehydroAla (1) where X and Y represent variable amino acids and Adda is 3-amino-9-methoxy-2,6,8-trimethyl-10-phenyldeca-4,6-dienoic acid (2). The structural studies on four variant toxins utilised n.m.r. and mass spectral methods analogous to those recently used to determine the structure of cyanoginosin-LA. [graphic omitted] (1)

Structural studies on cyanoginosins-LR, -YR, -YA, and -YM, peptide toxins from Microcystis aeruginosa

A detailed study of the mass spectra of peptides produced by the new technique of fast-atom bombardment is reported. Molecular weights of unmodified peptides containing up to 21 amino acids have been determined. In favourable cases, the molecular-weight determination may be made on as little as 0.1 nmol of sample. Positive-ion and negative-ion spectra are obtained with equal facility. With sample sizes in the range 2-50nmol, sequence information can be obtained in many cases. The technique represents an important contribution to structural studies on peptides, since (i) blocked peptides may be studied, (ii) no prior formation of chemical derivatives is necessary (except for distinction between lysine and glutamine), (iii) sensitivity is good, (iv) large peptides, and, in some cases, mixtures of peptides, can be studied, and (v) the technique is easy to operate, with ions being produced over a long period (5-30 min).

Sitthivet Santikarn

Papers

The structure of cyanoginosin-LA, a cyclic heptapeptide toxin from the cyanobacterium Microcystis aeruginosa

Identification of the NH2‐terminal blocking group of calcineurin B as myristic acid

Fast atom bombardment mass spectrometry: a powerful technique for the study of polar molecules

Structural studies on cyanoginosins-LR, -YR, -YA, and -YM, peptide toxins from Microcystis aeruginosa

Fast-atom-bombardment mass spectrometry. A new technique for the determination of molecular weights and amino acid sequences of peptides.